[具体物种]的几丁质酶系统及参与几丁质降解的酶的特性
Chitinase system of , and characterization of enzymes involved in chitin degradation.
作者信息
Pentekhina Iuliia, Hattori Tatsuyuki, Tran Dinh Minh, Shima Mizuki, Watanabe Takeshi, Sugimoto Hayuki, Suzuki Kazushi
机构信息
Graduate School of Science and Technology, Niigata University , Niigata, Japan.
School of Economics and Management, Far Eastern Federal University , Vladivostok, Russia.
出版信息
Biosci Biotechnol Biochem. 2020 Sep;84(9):1936-1947. doi: 10.1080/09168451.2020.1771539. Epub 2020 May 29.
The genes encoding chitin-degrading enzymes in SWSY-1.411 were identified and cloned in . The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC and AsChiD, and an auxiliary activities family 10 protein, lytic polysaccharide monooxygenase: AsLPMO10A. These enzymes were successfully expressed in and purified. AsChiB had the highest hydrolytic activity against insoluble chitin. AsChiD had the highest activity against water-soluble chitin. The peroxygenase activity of AsLPMO10A was lower compared to SmLPMO10A from . Synergism on powdered chitin degradation was observed when AsChiA and AsLPMO10A were combined with other chitinases of this strain. More than twice the increase of the synergistic effect was observed when powdered chitin was treated by a combination of AsLPMO10A with all chitinases. GH19 chitinases suppressed the hyphal growth of
在SWSY-1.411中编码几丁质降解酶的基因被鉴定并克隆。该菌株含有两个糖苷水解酶（GH）家族18的几丁质酶：AsChiA和AsChiB，两个GH19几丁质酶：AsChiC和AsChiD，以及一个辅助活性家族10蛋白，即裂解多糖单加氧酶：AsLPMO10A。这些酶在[具体表达宿主未给出]中成功表达并纯化。AsChiB对不溶性几丁质具有最高的水解活性。AsChiD对水溶性几丁质具有最高活性。与来自[具体菌株未给出]的SmLPMO10A相比，AsLPMO10A的过氧酶活性较低。当AsChiA和AsLPMO10A与该菌株的其他几丁质酶联合使用时，观察到对粉末状几丁质降解的协同作用。当用AsLPMO10A与所有几丁质酶组合处理粉末状几丁质时，观察到协同效应增加了两倍多。GH19几丁质酶抑制了[具体对象未给出]的菌丝生长
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